Abstract
Peptide-tag based labelling can be achieved by (i) enzymes (ii) recognition of metal ions or small molecules and (iii) peptide-peptide interactions and enables site-specific protein visualization to investigate protein localization and trafficking.
Highlights
Visualizing the localization and trafficking of proteins in living systems is the key to understand protein functions in their native environment
Phosphopantetheinyl transferases (PPTase) such as Sfp and AcpS catalyse the transfer of a phosphopantetheinyl (Ppant) group derived from coenzyme A (CoA) to a serine residue within a specific recognition sequence (Fig. 2A).[34]
Owing to an impressive substrate promiscuity of Sfp and AcpS, CoA can be modified at its terminal thiol with small molecules, including biotin, sugars, peptides, porphyrin and fluorophores, the latter allowing one-step labelling similar to lipoic acid ligase (LplA).[34,35,36,37]
Summary
Interfacing chemical biology with the -omic sciences and systems biology www.rsc.org/molecularbiosystems. Beck-Sickinger et al Peptide-tags for site-specific protein labelling in vitro and in vivo.
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